ArticleMolecular microbiology2014
Pbp2x localizes separately from Pbp2b and other peptidoglycan synthesis proteins during later stages of cell division of Streptococcus pneumoniae D39.
Article in Molecular microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers.
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72 citing papers in PubMed, 102 citations in OpenAlex.
- Penicillin-Binding Proteins inAntibiotics (Basel, Switzerland) · 2026Review
- Pneumococcal S protein coordinates cell wall modification and repair to resist host antimicrobials.Nature microbiology · 2026Article
- Streptococcus pneumoniae S protein activates PBP1a to regulate peptidoglycan remodelling and cell division.Nature microbiology · 2026Article
- The effect of MurM and a branched cell wall structure on penicillin resistance inJournal of bacteriology · 2025Article
- Transient inhibition of cell division in competent pneumococcal cells results from deceleration of the septal peptidoglycan complex.Nature communications · 2025Article
- Decoding the Penicillin-Binding Proteins with Activity-Based Probes.Accounts of chemical research · 2025Review
- Glycosylation of serine/threonine-rich intrinsically disordered regions of membrane-associated proteins in streptococci.Nature communications · 2025Article
- A high-resolution screen identifies a preexisting beta-lactam that specifically treats Lyme disease in mice.Science translational medicine · 2025Article
- How do spherical bacteria regulate cell division?Biochemical Society transactions · 2025Review
- Elongasome core proteins and class A PBP1a display zonal, processive movement at the midcell ofProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Spontaneous mutations and mutational responses to penicillin treatment in the bacterial pathogenMarine life science & technology · 2024Article
- Drug Discovery in the Field of β-Lactams: An Academic Perspective.Antibiotics (Basel, Switzerland) · 2024Review
- Negative regulation of MurZ and MurA underlies the essentiality of GpsB- and StkP-mediated protein phosphorylation in Streptococcus pneumoniae D39.Molecular microbiology · 2023Article
- DivIVA Interacts with the Cell Wall Hydrolase MltG To Regulate Peptidoglycan Synthesis in Streptococcus suis.Microbiology spectrum · 2023Article
- The divisome but not the elongasome organizes capsule synthesis in Streptococcus pneumoniae.Nature communications · 2023Article
- Synthesis of vancomycin fluorescent probes that retain antimicrobial activity, identify Gram-positive bacteria, and detect Gram-negative outer membrane damage.Communications biology · 2023Article
- Roles of RodZ and class A PBP1b in the assembly and regulation of the peripheral peptidoglycan elongasome in ovoid-shaped cells of Streptococcus pneumoniae D39.Molecular microbiology · 2022Article
- Amoxicillin-resistanteLife · 2022Article
- What Is Motion? Recent Advances in the Study of Molecular Movement Patterns of the Peptidoglycan Synthesis Machines.Journal of bacteriology · 2022Review
- The bacterial tyrosine kinase system CpsBCD governs the length of capsule polymers.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
12 more citing papers are in PubMed but not listed here.
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11 authors at 1 institution in 1 country.
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Abstract
The relative localization patterns of class B penicillin-binding proteins Pbp2x and Pbp2b were used as positional indicators of septal and peripheral (side-wall-like) peptidoglycan (PG) synthesis, respectively, in the mid-cell regions of Streptococcus pneumoniae cells at different stages of division. We confirm that Pbp2x and Pbp2b are essential in the strain D39 genetic background, which differs from that of laboratory strains. We show that Pbp2b, like Pbp2x and class A Pbp1a, follows a different localization pattern than FtsZ and remains at division septa after FtsZ reappears at the equators of daughter cells. Pulse-experiments with fluorescent D-amino acids (FDAAs) were performed in wild-type cells and in cells in which Pbp2x activity was preferentially inhibited by methicillin or Pbp2x amount was depleted. These experiments show that Pbp2x activity separates from that of other PBPs to the centres of constricting septa in mid-to-late divisional cells resolved by high-resolution 3D-SIM microscopy. Dual-protein and protein-fluorescent vancomycin 2D and 3D-SIM immunofluorescence microscopy (IFM) of cells at different division stages corroborate that Pbp2x separates to the centres of septa surrounded by an adjacent constricting ring containing Pbp2b, Pbp1a and regulators, StkP and MreC. The separate localization of Pbp2x suggests distinctive roles in completing septal PG synthesis and remodelling.
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